Research workbench
Spatial structure of insectotoxin I5A buthus eupeus by 1H nuclear magnetic resonance spectroscopy (russian)
Analyse Spatial structure of insectotoxin I5A buthus eupeus by 1H nuclear magnetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SIS
- Type
- protein
- Length
- 35 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Scorpion insectotoxin I5A
- UniProt
- P15222
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 23% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Scorpion insectotoxin I5A | protein | 35 | 23% helix, 29% strand | P15222 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1SIS · Spatial structure of insectotoxin I5A buthus eupeus by 1H nuclear magnetic resonance… · the same entry in another collection · chain A against A, TM-score 1.00
- P15222 · AlphaFold monomer V2.0 prediction for insectotoxin-I5A (P15222) · a predicted model of the same protein · chain A against A, TM-score 0.73
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P15222
- Elsewhere: RCSB PDB 1SIS · PDBe 1SIS · UniProt P15222
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